6B3R

Structure of the mechanosensitive channel Piezo1

Summary for 6B3R

• Entry DOI: 10.2210/pdb6b3r/pdb
• EMDB information: 7042
• Descriptor: Piezo-type mechanosensitive ion channel component 1, Piezo-type mechanosensitive ion channel component 1, unknown fragment (2 entities in total)
• Functional Keywords: triskelion, transmembrane, ion channel, membrane protein, transport protein
• Biological source: Mus musculus (Mouse); More
• Cellular location: Endoplasmic reticulum membrane ; Multi-pass membrane protein: E2JF22
• Total number of polymer chains: 6
• Total formula weight: 881101.04

Authors

Guo, Y.R.,MacKinnon, R. (deposition date: 2017-09-22, release date: 2017-12-20, Last modification date: 2024-10-23)

Primary citation

Guo, Y.R.,MacKinnon, R.
Structure-based membrane dome mechanism for Piezo mechanosensitivity.
Elife, 6:-, 2017

PubMed Abstract: Mechanosensitive ion channels convert external mechanical stimuli into electrochemical signals for critical processes including touch sensation, balance, and cardiovascular regulation. The best understood mechanosensitive channel, MscL, opens a wide pore, which accounts for mechanosensitive gating due to in-plane area expansion. Eukaryotic Piezo channels have a narrow pore and therefore must capture mechanical forces to control gating in another way. We present a cryo-EM structure of mouse Piezo1 in a closed conformation at 3.7Å-resolution. The channel is a triskelion with arms consisting of repeated arrays of 4-TM structural units surrounding a pore. Its shape deforms the membrane locally into a dome. We present a hypothesis in which the membrane deformation changes upon channel opening. Quantitatively, membrane tension will alter gating energetics in proportion to the change in projected area under the dome. This mechanism can account for highly sensitive mechanical gating in the setting of a narrow, cation-selective pore.

PubMed: 29231809
DOI: 10.7554/eLife.33660

Experimental method

ELECTRON MICROSCOPY (3.8 Å)